EFM7_CANGA
ID EFM7_CANGA Reviewed; 256 AA.
AC Q6FJ22;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein N-terminal and lysine N-methyltransferase EFM7 {ECO:0000255|HAMAP-Rule:MF_03223};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03223};
DE AltName: Full=Elongation factor methyltransferase 7 {ECO:0000255|HAMAP-Rule:MF_03223};
GN Name=EFM7 {ECO:0000255|HAMAP-Rule:MF_03223}; Synonyms=NNT1;
GN OrderedLocusNames=CAGL0M09801g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein methyltransferase
CC that trimethylates the N-terminal glycine 'Gly-2' of elongation factor
CC 1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
CC {ECO:0000255|HAMAP-Rule:MF_03223}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03223}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM7 family. {ECO:0000255|HAMAP-Rule:MF_03223}.
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DR EMBL; CR380959; CAG62750.1; -; Genomic_DNA.
DR RefSeq; XP_449772.1; XM_449772.1.
DR AlphaFoldDB; Q6FJ22; -.
DR SMR; Q6FJ22; -.
DR STRING; 5478.XP_449772.1; -.
DR EnsemblFungi; CAG62750; CAG62750; CAGL0M09801g.
DR GeneID; 2891336; -.
DR KEGG; cgr:CAGL0M09801g; -.
DR CGD; CAL0136847; CAGL0M09801g.
DR VEuPathDB; FungiDB:CAGL0M09801g; -.
DR eggNOG; KOG2920; Eukaryota.
DR HOGENOM; CLU_032409_0_0_1; -.
DR InParanoid; Q6FJ22; -.
DR OMA; YQPWLLP; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; IEA:UniProtKB-UniRule.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; IEA:UniProtKB-UniRule.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03223; Methyltr_EFM7; 1.
DR InterPro; IPR025784; EFM7.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51560; SAM_MT_NNT1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..256
FT /note="Protein N-terminal and lysine N-methyltransferase
FT EFM7"
FT /id="PRO_0000096892"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT BINDING 90..92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT BINDING 112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT BINDING 168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
SQ SEQUENCE 256 AA; 29176 MW; 3EA9B15469C66D21 CRC64;
MSDTESLNDA LGLFDEPEDF RPEKPKEHYA NYERIDVPDI SKSKITNLKL QLVGSSPLWG
HLLWNAGIYT ARHLDKYPEL VSNKNVLELG AASALPSLVA GLIGAKRAVV TDYPDADLMA
NIQYNVNTII PDELKENVRV EGYIWGNEYD PLTIHLDGDK KFDLIILSDL VFNHNQHDKL
LQTTKDLLAT NGKALVVFSP HRPHLLEADL QFFETCKEYG LTPEKIEMVN WKPMFEEDEE
TAEVRSRVYA YYMTHA
